1iij

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[[Image:1iij.jpg|left|200px]]
[[Image:1iij.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1iij |SIZE=350|CAPTION= <scene name='initialview01'>1iij</scene>
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The line below this paragraph, containing "STRUCTURE_1iij", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] </span>
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{{STRUCTURE_1iij| PDB=1iij | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iij OCA], [http://www.ebi.ac.uk/pdbsum/1iij PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iij RCSB]</span>
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'''SOLUTION STRUCTURE OF THE NEU/ERBB-2 MEMBRANE SPANNING SEGMENT'''
'''SOLUTION STRUCTURE OF THE NEU/ERBB-2 MEMBRANE SPANNING SEGMENT'''
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==About this Structure==
==About this Structure==
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1IIJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIJ OCA].
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1IIJ is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIJ OCA].
==Reference==
==Reference==
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[[Category: Dufourc, E J.]]
[[Category: Dufourc, E J.]]
[[Category: Goetz, M.]]
[[Category: Goetz, M.]]
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[[Category: alpha-helix-pi-bulge-alpha-helix]]
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[[Category: Alpha-helix-pi-bulge-alpha-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:02:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:20:15 2008''
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Revision as of 17:02, 2 May 2008

Template:STRUCTURE 1iij

SOLUTION STRUCTURE OF THE NEU/ERBB-2 MEMBRANE SPANNING SEGMENT


Overview

The 35-residue peptide corresponding to the very hydrophobic transmembrane region of the tyrosine kinase receptor neu, Neu(TM35), has been synthesized. The peptide can be solubilized in millimolar concentrations in TFE or incorporated into an SDS-water micellar solution or into well-hydrated DMPC/DCPC bicelles. In all these media, circular dichroism demonstrated that the peptide adopts a helical structure for about 80% of its amino acids. The peptide is monomeric below 2 mM in TFE, as also determined by variable concentration experiments. The three-dimensional solution structure in TFE has been obtained by homonuclear proton NMR and shows a well-defined alpha-helix from residues 4 to 21, then a pi-bulge from Ile(22) to Gly(28), and a final short alpha-helix from positions 29 to 32. This experimental finding is in agreement with structures predicted recently by molecular dynamics calculations in a vacuum [Sajot, N., and Genest, M. (2000) Eur. Biophys. J. 28, 648-662]. The biological implications of a possible retention of this structure in a membrane environment are finally discussed.

About this Structure

1IIJ is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Evidence for an alpha-helix --> pi-bulge helicity modulation for the neu/erbB-2 membrane-spanning segment. A 1H NMR and circular dichroism study., Goetz M, Carlotti C, Bontems F, Dufourc EJ, Biochemistry. 2001 May 29;40(21):6534-40. PMID:11371217 Page seeded by OCA on Fri May 2 20:02:29 2008

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